Molecular cloning and sequence analysis of the murine cDNA for the cystic fibrosis transmembrane conductance regulator

Genomics. 1991 Jul;10(3):547-50. doi: 10.1016/0888-7543(91)90434-g.


We have cloned the mouse homolog of the human cystic fibrosis transmembrane conductance regulator (CFTR) using clones isolated from a mouse lung cDNA library and using amplification of cDNA to isolate specific regions. The cDNA was 6304 bp in length and encoded a polypeptide of 1476 amino acids. Comparison of the deduced amino acid sequence showed that the mouse protein has high homology to the human protein; overall identity was 78.3%. The amino acid identity was high for both transmembrane domains (first transmembrane domain, 86.7%; second transmembrane domain, 81.1%) and for both ATP-binding folds (first ATP-binding fold, 80.5%; second ATP-binding fold, 83.9%), suggesting the functional importance of these regions. On the other hand, the R domain was less well conserved (68.9% identity). All of the published missense mutation sites and the site of the common delta F508 mutation were conserved between human and mouse.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cystic Fibrosis Transmembrane Conductance Regulator
  • DNA / genetics
  • Genes
  • Humans
  • Membrane Proteins / genetics*
  • Mice / genetics*
  • Molecular Sequence Data
  • Sequence Homology, Nucleic Acid
  • Species Specificity


  • CFTR protein, human
  • Membrane Proteins
  • Cystic Fibrosis Transmembrane Conductance Regulator
  • DNA